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  • 1
    Publication Date: 1987-01-16
    Description: Autoimmune sera of the Sm specificity react with the major class of small nuclear RNA (snRNA)-containing ribonucleoprotein particles (snRNP's) from organisms as evolutionarily divergent as insects and dinoflagellates but have been reported not to recognize snRNP's from yeast. The Sm antigen is thought to bind to a conserved snRNA motif that includes the sequence A(U3-6)G. The hypothesis was tested that yeast also contains functional analogues of Sm snRNA's, but that the Sm binding site in the RNA is more strictly conserved than the Sm antigenic determinant. After microinjection of labeled yeast snRNA's into Xenopus eggs or oocytes, two snRNA's from Saccharomyces cerevisiae become strongly immunoprecipitable with human auto-antibodies known as anti-Sm. These each contain the sequence A(U5-6)G, are essential for viability, and are constituents of the spliceosome. At least six other yeast snRNA's do not become immunoprecipitable and lack this sequence; these non-Sm snRNA's are all dispensable.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riedel, N -- Wolin, S -- Guthrie, C -- GM 21119/GM/NIGMS NIH HHS/ -- GM 26875/GM/NIGMS NIH HHS/ -- GM 31286/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 16;235(4786):328-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2948278" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoantigens/*metabolism ; Binding Sites ; Protein Binding ; RNA, Small Nuclear/*metabolism ; Ribonucleoproteins/*metabolism ; Ribonucleoproteins, Small Nuclear ; Saccharomyces cerevisiae/*genetics/immunology ; Xenopus laevis ; snRNP Core Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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